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Journal articles on the topic 'NanoLC FT MS/MS'

Author: Grafiati

Published: 29 April 2023

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1

Umar, Arzu, Theo M. Luider, John A. Foekens, and Ljiljana Paša-Tolić. "NanoLC-FT-ICR MS improves proteome coverage attainable for ∼3000 laser-microdissected breast carcinoma cells." PROTEOMICS 7, no. 2 (January 2007): 323–29. http://dx.doi.org/10.1002/pmic.200600293.

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Lakshmanan, Rajeswari, Jeremy J. Wolff, Rudy Alvarado, and Joseph A. Loo. "Top-down protein identification of proteasome proteins with nanoLC-FT-ICR-MS employing data-independent fragmentation methods." PROTEOMICS 14, no. 10 (March 26, 2014): 1271–82. http://dx.doi.org/10.1002/pmic.201300339.

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3

Barnes, Stephen, Erin M. Shonsey, Shannon M. Eliuk, David Stella, Kerri Barrett, Om P. Srivastava, Helen Kim, and Matthew B. Renfrow. "High-resolution mass spectrometry analysis of protein oxidations and resultant loss of function." Biochemical Society Transactions 36, no. 5 (September 19, 2008): 1037–44. http://dx.doi.org/10.1042/bst0361037.

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MS, with or without pre-analysis peptide fractionation, can be used to decipher the residues on proteins where oxidative modifications caused by peroxynitrite, singlet oxygen or electrophilic lipids have occurred. Peroxynitrite nitrates tyrosine and tryptophan residues on the surface of actin. Singlet oxygen, formed by the interaction of UVA light with tryptophan, can oxidize neighbouring cysteine, histidine, methionine, tyrosine and tryptophan residues. Dose–response inactivation by 4HNE (4-hydroxynonenal) of hBAT (human bile acid CoA:amino acid N-acyltransferase) and CKBB (cytosolic brain isoform of creatine kinase) is associated with site-specific modifications. FT-ICR (Fourier-transform ion cyclotron resonance)–MS using nanoLC (nano-liquid chromatography)–ESI (electrospray ionization)–MS or direct-infusion ESI–MS with gas-phase fractionation identified 14 4HNE adducts on hBAT and 17 on CKBB respectively. At 4HNE concentrations in the physiological range, one member of the catalytic triad of hBAT (His362) was modified; for CKBB, although all four residues in the active site that were modifiable by 4HNE were ultimately modified, only one, Cys283, occurred at physiological concentrations of 4HNE. These results suggest that future in vivo studies should carefully assess the critical sites that are modified rather than using antibodies that do not distinguish between different modified sites.

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Chew, H. K., S. Miyamoto, H. An, D. Rocke, and C. Lebrilla. "Serum glycan analysis in metastatic breast cancer." Journal of Clinical Oncology 25, no. 18_suppl (June 20, 2007): 11504. http://dx.doi.org/10.1200/jco.2007.25.18_suppl.11504.

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11504 Background: There is a need for a reliable breast cancer biomarker that can predict a patient’s response to therapy. Serum glycans, or oligosaccharides, are of particular interest as over half of all proteins are glycosylated and alterations in glycosylation influence growth, adhesion, metastasis and immune surveillance of tumor, among other important functions. Serum glycans can be analyzed by high resolution mass spectrometry. Methods: Sera from patients with known metastatic breast cancer and age-matched healthy controls without medical problems were prospectively analyzed by mass spectroscopy. Women over the age of 18, who were not pregnant or breastfeeding, and who were without other active cancers were eligible. Samples were de-identified for laboratory personnel who analyzed sera by matrix-assisted laser desoprtion/ionization (MALDI) and Fourier transform ion-cyclotron resonance mass sepctrometry (FT ICR MS). Glycans were also profiled by chromatographic separation using a microchip nanoLC (Agilent) with a time-of-flight (TOF) mass analyzers. Results: Sera from 25 patients with metastatic breast cancer and 25 controls were evaluated. The mass profiles were obtained corresponding to both N-linked oligosaccharides (N-glycans) and O-linked oligosaccharides (O-glycans). Distinct variations in glycosylation were observed among sera analyzed from patients with metastatic breast cancer compared to controls. Specific glycan masses were analyzed and found to correspond to N-glycans. The chromatographic glycan profile showed individual glycans that were distinct for the cancer patients. Conclusions: Analysis of serum gylcans by mass spectrometry represents a new paradigm of cancer biomarker studies, focusing on post-translational modifications of proteins, rather than protein expression. Further refinement of this technology may be clinically useful in monitoring response to therapy in metastatic breast cancer. No significant financial relationships to disclose.

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5

Koch, Heiner, Gary Kruppa, and Rohan Thakur. "Plasma Proteomics with NanoLC-MS." Genetic Engineering & Biotechnology News 39, no. 7 (July 2019): 52–54. http://dx.doi.org/10.1089/gen.39.07.15.

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6

Stolz, Alexander, and Christian Neusüß. "Characterisation of a new online nanoLC-CZE-MS platform and application for the glycosylation profiling of alpha-1-acid glycoprotein." Analytical and Bioanalytical Chemistry 414, no. 5 (December 9, 2021): 1745–57. http://dx.doi.org/10.1007/s00216-021-03814-6.

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AbstractThe ever-increasing complexity of biological samples to be analysed by mass spectrometry has led to the necessity of sophisticated separation techniques, including multidimensional separation. Despite a high degree of orthogonality, the coupling of liquid chromatography (LC) and capillary zone electrophoresis (CZE) has not gained notable attention in research. Here, we present a heart-cut nanoLC-CZE-ESI-MS platform to analyse intact proteins. NanoLC and CZE-MS are coupled using a four-port valve with an internal nanoliter loop. NanoLC and CZE-MS conditions were optimised independently to find ideal conditions for the combined setup. The valve setup enables an ideal transfer efficiency between the dimensions while maintaining good separation conditions in both dimensions. Due to the higher loadability, the nanoLC-CZE-MS setup exhibits a 280-fold increased concentration sensitivity compared to CZE-MS. The platform was used to characterise intact human alpha-1-acid glycoprotein (AGP), an extremely heterogeneous N-glycosylated protein. With the nanoLC-CZE-MS approach, 368 glycoforms can be assigned at a concentration of 50 μg/mL as opposed to the assignment of only 186 glycoforms from 1 mg/mL by CZE-MS. Additionally, we demonstrate that glycosylation profiling is accessible for dried blood spot analysis (25 μg/mL AGP spiked), indicating the general applicability of our setup to biological matrices. The combination of high sensitivity and orthogonal selectivity in both dimensions makes the here-presented nanoLC-CZE-MS approach capable of detailed characterisation of intact proteins and their proteoforms from complex biological samples and in physiologically relevant concentrations. Graphical abstract

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7

McClung, Colleen, Hang Gyeong Chin, Ulla Hansen, Christopher J. Noren, Sriharsa Pradhan, and Cristian I. Ruse. "Mapping of polyglutamylation in tubulins using nanoLC-ESI-MS/MS." Analytical Biochemistry 612 (January 2021): 113761. http://dx.doi.org/10.1016/j.ab.2020.113761.

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8

Bag, Swarnendu, Debabrata Dutta, Amrita Chaudhary, Bidhan Chandra Sing, Rita Banerjee, Mousumi Pal, Ranjan Rashmi Paul, et al. "NanoLC MALDI MS/MS based quantitative metabolomics reveals the alteration of membrane biogenesis in oral cancer." RSC Advances 6, no. 67 (2016): 62420–33. http://dx.doi.org/10.1039/c6ra07001a.

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9

Li, Haiying, Stephen A. Kostel, Shannon E. DiMartino, Ali Hashemi Gheinani, John W. Froehlich, and Richard S. Lee. "Uromodulin Isolation and Its N-Glycosylation Analysis by NanoLC-MS/MS." Journal of Proteome Research 20, no. 5 (March 2, 2021): 2662–72. http://dx.doi.org/10.1021/acs.jproteome.0c01053.

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10

Boutin, Michel, Carl Berthelette, François G. Gervais, Mary-Beth Scholand, John Hoidal, Mark F. Leppert, Kevin P. Bateman, and Pierre Thibault. "High-Sensitivity NanoLC−MS/MS Analysis of Urinary Desmosine and Isodesmosine." Analytical Chemistry 81, no. 5 (March 2009): 1881–87. http://dx.doi.org/10.1021/ac801745d.

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11

Shen, Yufeng, Nikola Tolić, Christophe Masselon, Ljiljana Paša-Tolić, David G. Camp, Kim K. Hixson, Rui Zhao, Gordon A. Anderson, and Richard D. Smith. "Ultrasensitive Proteomics Using High-Efficiency On-Line Micro-SPE-NanoLC-NanoESI MS and MS/MS." Analytical Chemistry 76, no. 1 (January 2004): 144–54. http://dx.doi.org/10.1021/ac030096q.

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12

Pozzi, D., G. Caracciolo, A. L. Capriotti, C. Cavaliere, S. Piovesana, V. Colapicchioni, S. Palchetti, A. Riccioli, and A. Laganà. "A proteomics-based methodology to investigate the protein corona effect for targeted drug delivery." Mol. BioSyst. 10, no. 11 (2014): 2815–19. http://dx.doi.org/10.1039/c4mb00292j.

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13

Lin, Xionghao, Elena Afia Adjei, Namita Kumari, Sharmin Diaz, Marina Jerebtsova, Patricia A. Oneal, and Sergei Nekhai. "Semi-Automatic Enrichment with High Resolution/Selected Reaction Monitoring (HR/SRM) Scan for the Detection of Urinary Hepcidin in Patients with Sickle Cell Disease." Blood 126, no. 23 (December 3, 2015): 3418. http://dx.doi.org/10.1182/blood.v126.23.3418.3418.

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Abstract Background Urinary hepcidin is a potential biomarker of renal inflammation and acute kidney injury (AKI) which is elevated in sickle cell disease (SCD). Hepcidin in circulation is filtered through glomeruli filtration barrier and reabsorbed by the renal tubules. Hepcidin can also be synthesized by the kidney tubular cells. Thus, increased urinary levels of hepcidin may reflect either a reduction in tubular uptake or an increase in renal production. Recent studies suggested that urinary hepcidin may protect against AKI by attenuating heme-mediated injury. Thus decreased hepcidin levels in SCD patients may contribute to AKI and serve as potentially informative marker of SCD-associated kidney injury. Previously, hepcidin was measured by ELISA and mass spectrometry. Immunoassays are limited due to the cross-reactivity of antibodies to prohepcidin and truncated hepcidin-20, -22, and -24 isoforms of active hepcidin-25. Mass spectrometric assays are specific for hepcidin-25 but sample preparation remains a challenge. Objective To develop a sensitive, reliable and reproducible nanoLC/FT-MS method with simplified sample preparation for measuring of hepcidin in urine samples. Also to correlate urinary hepcidin with urinary albumin and urinary protein to access the degree of kidney dysfunction. Methods Samples were enriched and purified semi-automaticaly on 10-uL ZipTip and online trap column. Stable isotope-labeled hepcidin was used as internal standard. The standard concentration range was 1.56-800 nM and quality control samples were 5 nM, 20 nM, 80 nM and 400 nM. Samples were subjected to an LC-20AD nano HPLC system coupled to an LTQ XL™ Orbitrap mass spectrometer with an in-house made nano-HPLC column. High resolution/selected reaction monitoring (HR/SRM) scan was carried out and the narrow mass range ([M+H]+ ±0.01 Da) was used to extract ion chromatograms (EICs) for quantification. Urinary samples were collected from 20 SCD patients and 13 controls. Urinary albumin, protein and creatinine were detected by ELISA. The urine hepcidin concentrations were normalized to urine creatinine (Cr) values. Results Semi-automatic approach simplified sample preparation and accelerated the analysis. At least 24 samples could be prepared and processed at the same time. Online column trapping further purified and enriched hepcidin and improved the sensitivity and specificity of this method by eliminating interferences from urine. Hepcidin showed a good linearity within the concentration range of 1.56-800 nM with an r2 value of 0.9994. The precision intraday (n = 5) and interday (n = 5) and the repeatability (n=5) of the method were good with relative standard deviations (RSDs) lower than 5%. The analyzed samples were stable for 3 days at +4°C (RSDs<5%). The percent mean recoveries of hepcidin was within the acceptable range of 89.65-104.79%. We found that SCD patients had significantly lower (about 2-fold) urinary hepcidin levels compared to controls, and urinary hepcidin levels in 2 SCD patients were below the lower limit of detection (<0.5 nM). We found that there was no difference in urine albumin between SCD and control subjects, total urine protein was significantly increased in SCD patients. There was no positive correlation between urine hepcidin and urine albumin or total protein. Conclusion We developed an LC-MS based method for measuring levels of urinary hepcidin. This method is promising in terms of recovery, sensitivity, selectivity, repeatability and simplicity of sample preparation. SCD patients showed significantly decreased hepcidin levels in urine suggesting a potentially novel mechanism of AKI in SCD. Acknowledgments This work was supported by NIH Research Grants (1P50HL118006, 1R01HL125005 and 5G12MD007597). The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health. Disclosures No relevant conflicts of interest to declare.

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Maasz, Gabor, Janos Schmidt, Peter Avar, and Laszlo Mark. "Automated SPE and nanoLC–MS analysis of somatostatin." Journal of Liquid Chromatography & Related Technologies 40, no. 8 (May 8, 2017): 400–406. http://dx.doi.org/10.1080/10826076.2017.1315722.

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15

Roberg-Larsen, Hanne, Caroline Vesterdal, Steven Ray Wilson, and Elsa Lundanes. "Underivatized oxysterols and nanoLC–ESI-MS: A mismatch." Steroids 99 (July 2015): 125–30. http://dx.doi.org/10.1016/j.steroids.2015.01.023.

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16

Orsburn, Benjamin C., Sierra D. Miller, and Conor J. Jenkins. "Standard Flow Multiplexed Proteomics (SFloMPro)—An Accessible Alternative to NanoFlow Based Shotgun Proteomics." Proteomes 10, no. 1 (January 13, 2022): 3. http://dx.doi.org/10.3390/proteomes10010003.

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Multiplexed proteomics using isobaric tagging allows for simultaneously comparing the proteomes of multiple samples. In this technique, digested peptides from each sample are labeled with a chemical tag prior to pooling sample for LC-MS/MS with nanoflow chromatography (NanoLC). The isobaric nature of the tag prevents deconvolution of samples until fragmentation liberates the isotopically labeled reporter ions. To ensure efficient peptide labeling, large concentrations of labeling reagents are included in the reagent kits to allow scientists to use high ratios of chemical label per peptide. The increasing speed and sensitivity of mass spectrometers has reduced the peptide concentration required for analysis, leading to most of the label or labeled sample to be discarded. In conjunction, improvements in the speed of sample loading, reliable pump pressure, and stable gradient construction of analytical flow HPLCs has continued to improve the sample delivery process to the mass spectrometer. In this study we describe a method for performing multiplexed proteomics without the use of NanoLC by using offline fractionation of labeled peptides followed by rapid “standard flow” HPLC gradient LC-MS/MS. Standard Flow Multiplexed Proteomics (SFloMPro) enables high coverage quantitative proteomics of up to 16 mammalian samples in about 24 h. In this study, we compare NanoLC and SFloMPro analysis of fractionated samples. Our results demonstrate that comparable data is obtained by injecting 20 µg of labeled peptides per fraction with SFloMPro, compared to 1 µg per fraction with NanoLC. We conclude that, for experiments where protein concentration is not strictly limited, SFloMPro is a competitive approach to traditional NanoLC workflows with improved up-time, reliability and at a lower relative cost per sample.

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17

Mohammed, Shabaz, Karsten Kraiczek, Martijn W. H. Pinkse, Simone Lemeer, Joris J. Benschop, and Albert J. R. Heck. "Chip-Based Enrichment and NanoLC−MS/MS Analysis of Phosphopeptides from Whole Lysates." Journal of Proteome Research 7, no. 4 (April 2008): 1565–71. http://dx.doi.org/10.1021/pr700635a.

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18

Schuhmann, Kai, Henrik Thomas, Jacobo Miranda Ackerman, Konstantin O. Nagornov, Yury O. Tsybin, and Andrej Shevchenko. "Intensity-Independent Noise Filtering in FT MS and FT MS/MS Spectra for Shotgun Lipidomics." Analytical Chemistry 89, no. 13 (June 15, 2017): 7046–52. http://dx.doi.org/10.1021/acs.analchem.7b00794.

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19

Nišavić, Marija, Goran V. Janjić, Amela Hozić, Marijana Petković, Miloš K. Milčić, Zoran Vujčić, and Mario Cindrić. "Positive and negative nano-electrospray mass spectrometry of ruthenated serum albumin supported by docking studies: an integrated approach towards defining metallodrug binding sites on proteins." Metallomics 10, no. 4 (2018): 587–94. http://dx.doi.org/10.1039/c7mt00330g.

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20

Wöhlbrand, Lars, Ralf Rabus, Bernd Blasius, and Christoph Feenders. "Influence of NanoLC Column and Gradient Length as well as MS/MS Frequency and Sample Complexity on Shotgun Protein Identification of Marine Bacteria." Journal of Molecular Microbiology and Biotechnology 27, no. 3 (2017): 199–212. http://dx.doi.org/10.1159/000478907.

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Protein identification by shotgun proteomics, i.e., nano-liquid chromatography (nanoLC) peptide separation online coupled to electrospray ionization (ESI) mass spectrometry (MS)/MS, is the most widely used gel-free approach in proteome research. While the mass spectrometer accounts for mass accuracy and MS/MS frequency, the nanoLC setup and gradient time influence the number of peptides available for MS analysis, which ultimately determine the number of proteins identifiable. Here, we report on the influence of (i) analytical column length (15, 25, or 50 cm) coupled to (ii) the applied gradient length (120, 240, 360, 480, or 600 min), as well as (iii) MS/MS frequency on peptide/protein identification by shotgun proteomics of (iv) 2 marine bacteria. Longer gradients increased the number of peptides/proteins identified as well as the reproducibility of identification. Furthermore, longer analytical columns strictly enlarge the covered proteome complement. Notably, the proteome complement identified with a short column and applying a long gradient is also covered when using longer columns with shorter gradients. Coverage of the proteome complement further increases with higher MS/MS frequency. Compilation of peptide lists of replicate analyses (same gradient length) improves protein identification, while compilation of analyses with different gradient lengths yields a similar or even higher number of proteins using comparable or even less total analysis time.

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Levin, Yishai, Julian A. J. Jaros, Emanuel Schwarz, and Sabine Bahn. "Multidimensional protein fractionation of blood proteins coupled to data-independent nanoLC–MS/MS analysis." Journal of Proteomics 73, no. 3 (January 2010): 689–95. http://dx.doi.org/10.1016/j.jprot.2009.10.013.

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22

Jou, Yu-Jen, Chun-Hung Hua, Chia-Der Lin, Chih-Ho Lai, Su-Hua Huang, Ming-Hsui Tsai, Jung-Yie Kao, and Cheng-Wen Lin. "S100A8 as potential salivary biomarker of oral squamous cell carcinoma using nanoLC–MS/MS." Clinica Chimica Acta 436 (September 2014): 121–29. http://dx.doi.org/10.1016/j.cca.2014.05.009.

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23

Onisko, Bruce, Irina Dynin, Jesús R. Requena, Christopher J. Silva, Melissa Erickson, and John Mark Carter. "Mass spectrometric detection of attomole amounts of the prion protein by nanoLC/MS/MS." Journal of the American Society for Mass Spectrometry 18, no. 6 (June 2007): 1070–79. http://dx.doi.org/10.1016/j.jasms.2007.03.009.

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24

Bonneil, Eric, Sylvain Tessier, Alain Carrier, and Pierre Thibault. "Multiplex multidimensional nanoLC-MS system for targeted proteomic analyses." ELECTROPHORESIS 26, no. 24 (December 2005): 4575–89. http://dx.doi.org/10.1002/elps.200500603.

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Gabriella Gulyás, Béla Béri, András Jávor, László Márk, Éva Csősz, Krisztina Pohóczky, Beáta Soltész, Dániel Kuti, and Levente Czeglédi. "Analysis of longevity in Holstein Friesian cattle using proteomic approaches." Acta Agraria Debreceniensis, no. 48 (July 31, 2012): 21–25. http://dx.doi.org/10.34101/actaagrar/48/2447.

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The aim of the present study was to determine marker proteins those are associated with functional longevity of dairy cattle. Holstein-Friesian cows were grouped based on their performance as follows: group 1) individuals with good longevity traits; group 2) short production life because of poor reproduction traits; group 3) short production life with low milk yield. Twelve individuals were sampled in each group, blood and milk samples were collected from cows. Blood samples were analysed with two dimensional polyacrylamide gel electrophoresis (2D PAGE), MALDI TOF/TOF and nanoLCMS/MS. The milk samples were analysed with MALDI TOF/TOF and nanoLC-MS/MS. Using the optimized gel based proteomic approach,we have succesfully separated 143 proteins in the group1, 139 proteins in the group2 and 136 proteins in the group3, but we could not find significant differences between groups in the expression pattern. Using MALDI TOF/TOF and nanoLC-IonTrap MS, we have found eleven protein sequences those were expressed only in the samples of good longevity group.

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Luo, Quanzhou, Jason S. Page, Keqi Tang, and Richard D. Smith. "MicroSPE-nanoLC-ESI-MS/MS Using 10-μm-i.d. Silica-Based Monolithic Columns for Proteomics." Analytical Chemistry 79, no. 2 (January 2007): 540–45. http://dx.doi.org/10.1021/ac061603h.

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27

Prenni, Jessica E., Zhouxin Shen, Sunia Trauger, Wei Chen, and Gary Siuzdak. "Protein characterization using Liquid Chromatography Desorption Ionization on Silicon Mass Spectrometry (LC-DIOS-MS)." Spectroscopy 17, no. 4 (2003): 693–98. http://dx.doi.org/10.1155/2003/172838.

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This paper presents a novel combination of of-line liquid chromatography (LC) separation with desorption ionization on silicon mass spectrometry (DIOS-MS) as an alternative to the traditional on-line coupling of LC and electrospray ionization (ESI). In this work, electrospray deposition is used to generate a spatially preserved linear track of the separated sample on a specially designed DIOS chip. The total sequence coverage analysis of two model protein systems was evaluated by both LC-DIOS-MS and nanoLC ESI tandem MS (MS/MS). LC-DIOS-MS yielded improved sequence coverage for both of the model systems (between 99.5 and 100%) compared with traditional LC-ESI-MS/MS analysis (between 82 and 87.6%). In addition to improved sequence coverage determination, LC-DIOS-MS also offers the potential for high-throughput protein characterization.

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Zhang, Qiwei, Xiaojun Feng, Henghui Li, Bi-Feng Liu, Yawei Lin, and Xin Liu. "Methylamidation for Isomeric Profiling of Sialylated Glycans by NanoLC-MS." Analytical Chemistry 86, no. 15 (July 21, 2014): 7913–19. http://dx.doi.org/10.1021/ac501844b.

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Humphrey, Sean J., Ben Crossett, and Benjamin L. Parker. "NanoBlow: A Simple Device To Limit Contaminants during NanoLC-MS." Journal of Proteome Research 18, no. 8 (June 24, 2019): 3219–22. http://dx.doi.org/10.1021/acs.jproteome.9b00175.

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Burgt, Y. E. M., I. M. Taban, M. Konijnenburg, M. Biskup, M. C. Duursma, R. M. A. Heeren, A. Römpp, R. V. Nieuwpoort, and H. E. Bal. "Parallel processing of large datasets from NanoLC-FTICR-MS measurements." Journal of the American Society for Mass Spectrometry 18, no. 1 (January 2007): 152–61. http://dx.doi.org/10.1016/j.jasms.2006.09.005.

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Zvereva, I. O., N. B. Savelieva, P. V. Postnikov, Yu A. Efimova, and M. A. Dikunets. "APPROACHES TO CHORIONIC GONADOTROPIN QUANTITATIVE DETERMINATION IN ANTI-DOPING CONTROL." Fine Chemical Technologies 12, no. 1 (February 28, 2017): 64–75. http://dx.doi.org/10.32362/2410-6593-2017-12-1-64-75.

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The article presents the results of the first stage of development of a new quantitative method for human chorionic gonadotropin (hCG) determination by means of ultra-high performance liquid chromatography coupled to tandem mass spectrometry (UPLC-MS/MS) to uncover doping abuse by athletes. The identified tryptic peptides correspond to the most abundant hCG isoforms: the α- and β-subunits, the nicked and β-core fragment of the hormone. Identification and sequencing of specific fragments were performed with the use of nanoLC-MS/MS. A high resolution / high accuracy hybrid mass-spectrometer was applied. Optimization of mass-spectrometric determination of selected specific peptides was accomplished by UPLC-MS/MS. Quantitative evaluation of hCG using specific fragments determination by UPLC-MS/MS allows to detect corresponding hCG isoforms. This significantly increases the method specificity and decreases the probability of false-positive results.

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Xu, Dihui, Chengli Yu, Jiaojiao Wang, Qiru Fan, Zhenzhong Wang, Wei Xiao, Jinao Duan, Jing Zhou, and Hongyue Ma. "Ultrafiltration strategy combined with nanoLC-MS/MS based proteomics for monitoring potential residual proteins in TCMIs." Journal of Chromatography B 1178 (July 2021): 122818. http://dx.doi.org/10.1016/j.jchromb.2021.122818.

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Eckert, Stephan, Yun-Chien Chang, Florian P. Bayer, Matthew The, Peer-Hendrik Kuhn, Wilko Weichert, and Bernhard Kuster. "Evaluation of Disposable Trap Column nanoLC–FAIMS–MS/MS for the Proteomic Analysis of FFPE Tissue." Journal of Proteome Research 20, no. 12 (November 4, 2021): 5402–11. http://dx.doi.org/10.1021/acs.jproteome.1c00695.

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Hu, Lianghai, Xin Li, Xinning Jiang, Houjiang Zhou, Xiaogang Jiang, Liang Kong, Mingliang Ye, and Hanfa Zou. "Comprehensive Peptidome Analysis of Mouse Livers by Size Exclusion Chromatography Prefractionation and NanoLC−MS/MS Identification." Journal of Proteome Research 6, no. 2 (February 2007): 801–8. http://dx.doi.org/10.1021/pr060469e.

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Szymkowicz, Lisa, Derek J. Wilson, and D. Andrew James. "Development of a targeted nanoLC-MS/MS method for quantitation of residual toxins from Bordetella pertussis." Journal of Pharmaceutical and Biomedical Analysis 188 (September 2020): 113395. http://dx.doi.org/10.1016/j.jpba.2020.113395.

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Ndiaye, Massamba M., Ha Phuong Ta, Giovanni Chiappetta, and Joëlle Vinh. "On-Chip Sample Preparation Using a ChipFilter Coupled to NanoLC-MS/MS for Bottom-Up Proteomics." Journal of Proteome Research 19, no. 7 (April 28, 2020): 2654–63. http://dx.doi.org/10.1021/acs.jproteome.9b00832.

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Christie-Oleza, Joseph Alexander, Juana Maria Piña-Villalonga, Philippe Guerin, Guylaine Miotello, Rafael Bosch, Balbina Nogales, and Jean Armengaud. "Shotgun nanoLC-MS/MS proteogenomics to document MALDI-TOF biomarkers for screening new members of theRuegeriagenus." Environmental Microbiology 15, no. 1 (June 19, 2012): 133–47. http://dx.doi.org/10.1111/j.1462-2920.2012.02812.x.

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Li, Yangguang, Ti Wen, Minzhi Zhu, Lixin Li, Jun Wei, Xiaoli Wu, Mingzhou Guo, et al. "Glycoproteomic analysis of tissues from patients with colon cancer using lectin microarrays and nanoLC-MS/MS." Molecular BioSystems 9, no. 7 (2013): 1877. http://dx.doi.org/10.1039/c3mb00013c.

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Liu, Si, Yang Fu, Zhiwen Huang, Yuanyuan Liu, Bi-Feng Liu, Liming Cheng, and Xin Liu. "A comprehensive analysis of subclass-specific IgG glycosylation in colorectal cancer progression by nanoLC-MS/MS." Analyst 145, no. 8 (2020): 3136–47. http://dx.doi.org/10.1039/d0an00369g.

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Franciosi, Lorenza, Natalia Govorukhina, Fabrizia Fusetti, Bert Poolman, Monique E. Lodewijk, Wim Timens, Dirkje Postma, Nick ten Hacken, and Rainer Bischoff. "Proteomic analysis of human epithelial lining fluid by microfluidics-based nanoLC-MS/MS: A feasibility study." ELECTROPHORESIS 34, no. 18 (August 22, 2013): 2683–94. http://dx.doi.org/10.1002/elps.201300020.

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Vahur, Signe, Anu Teearu, Tõiv Haljasorg, Piia Burk, Ivo Leito, and Ivari Kaljurand. "Analysis of dammar resin with MALDI-FT-ICR-MS and APCI-FT-ICR-MS." Journal of Mass Spectrometry 47, no. 3 (March 2012): 392–409. http://dx.doi.org/10.1002/jms.2971.

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Oteri, Marianna, Giovanni Bartolomeo, Francesca Rigano, Juan Aspromonte, Emanuela Trovato, Giorgia Purcaro, Paola Dugo, Luigi Mondello, and Marco Beccaria. "Comprehensive Chemical Characterization of Chia (Salvia hispanica L.) Seed Oil with a Focus on Minor Lipid Components." Foods 12, no. 1 (December 21, 2022): 23. http://dx.doi.org/10.3390/foods12010023.

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Abstract:

A comprehensive chemical characterization of different lipid components, namely fatty acid composition after derivatization in fatty acid methyl esters (FAMEs), triacylglycerols (TAGs), phospholipids (PLs), free fatty acids (FFAs), sterols, carotenoids, tocopherols, and polyphenols in Chia seed oil, obtained by Soxhlet extraction, was reported. Reversed phase liquid chromatography (RP-LC) coupled to UV and mass spectrometry (MS) detectors was employed for carotenoids, polyphenols, and TAGs determination; normal phase-LC in combination with fluorescence detector (FLD) was used for tocopherols analysis; PL and FFA fractions were investigated after a rapid solid phase extraction followed by RP-LC-MS and NanoLC coupled to electron ionization (EI) MS, respectively. Furthermore, gas chromatography (GC)-flame ionization (FID) and MS detectors were used for FAMEs and sterols analysis. Results demonstrated a significant content of bioactive compounds, such as the antioxidant tocopherols (22.88 µg mL−1), and a very high content of essential fatty acids (81.39%), namely α-linolenic (62.16%) and linoleic (19.23%) acids. In addition, for the best of authors knowledge, FFA profile, as well as some carotenoid classes has been elucidated for the first time. The importance of free fatty acids in vegetable matrices is related to the fact that they can be readily involved in metabolic processes or biosynthetic pathways of the plant itself. For a fast and reliable determination of this chemical class, a very innovative and sensitive NanoLC-EI-MS analytical determination was applied.

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Köcher, Thomas, Peter Pichler, Remco Swart, and Karl Mechtler. "Analysis of protein mixtures from whole-cell extracts by single-run nanoLC-MS/MS using ultralong gradients." Nature Protocols 7, no. 5 (April 12, 2012): 882–90. http://dx.doi.org/10.1038/nprot.2012.036.

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White, Brittany L., Timothy H. Sanders, and Jack P. Davis. "Potential ACE-inhibitory activity and nanoLC-MS/MS sequencing of peptides derived from aflatoxin contaminated peanut meal." LWT - Food Science and Technology 56, no. 2 (May 2014): 537–42. http://dx.doi.org/10.1016/j.lwt.2013.11.039.

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Verleyen, Peter, Geert Baggerman, Wannes D’Hertog, Evy Vierstraete, Steven J. Husson, and Liliane Schoofs. "Identification of new immune induced molecules in the haemolymph of Drosophila melanogaster by 2D-nanoLC MS/MS." Journal of Insect Physiology 52, no. 4 (April 2006): 379–88. http://dx.doi.org/10.1016/j.jinsphys.2005.12.007.

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Kawashima, Yusuke, and Osamu Ohara. "Development of a NanoLC–MS/MS System Using a Nonporous Reverse Phase Column for Ultrasensitive Proteome Analysis." Analytical Chemistry 90, no. 21 (October 12, 2018): 12334–38. http://dx.doi.org/10.1021/acs.analchem.8b03382.

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Schulte, Fabian, Hatice Hasturk, and Markus Hardt. "Mapping Relative Differences in Human Salivary Gland Secretions by Dried Saliva Spot Sampling and nanoLC–MS/MS." PROTEOMICS 19, no. 20 (September 26, 2019): 1900023. http://dx.doi.org/10.1002/pmic.201900023.

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CUTILLAS, Pedro R., Anthony G. W. NORDEN, Rainer CRAMER, Alma L. BURLINGAME, and Robert J. UNWIN. "Detection and analysis of urinary peptides by on-line liquid chromatography and mass spectrometry: application to patients with renal Fanconi syndrome." Clinical Science 104, no. 5 (May 1, 2003): 483–90. http://dx.doi.org/10.1042/cs20020342.

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Abstract:

Urinary proteomics has become a topical and potentially valuable field of study in relation to normal and abnormal renal function. Filtered bioactive peptides present in high concentration in the nephron of patients with tubular proteinuria may have downstream effects on renal tubular function. In renal Fanconi syndromes, such as Dent's disease, peptides implicated in altered tubular function or injury have recently been measured in urine by immunochemical methods. However, the limited availability of antibodies means that only certain peptides can be detected in this way. We have used nanoflow liquid chromatography and tandem mass spectrometry (nanoLC-MS/MS) as a complementary technique to analyse urinary peptides. Urine was desalted by solid-phase extraction (SPE) and its peptides were then separated from neutral and acidic compounds by strong cation-exchange chromatography (SCX), which was also used to fractionate the peptide mixture. Fractions from the SCX step were separated further by reversed-phase LC and analysed on-line by MS/MS. Extraction by SPE showed a good recovery of small peptides. We detected over 100 molecular species in urine samples from three individuals with Dent's disease. In addition to plasma and known urinary proteins, we identified some novel proteins and potentially bioactive peptides in urine from these patients, which were not present in normal urine. These data show that nanoLC-MS/MS complements existing techniques for the identification of polypeptides in urine. This approach is a potentially powerful tool to discover new markers and/or causative factors in renal disease; in addition, its sensitivity may also make it applicable to the direct ultramicroanalysis of renal tubule fluid.

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Das, Rajdeep, Gopa Mitra, Boby Mathew, Cecil Ross, Vijay Bhat, and Amit Kumar Mandal. "Automated Analysis of Hemoglobin Variants Using NanoLC–MS and Customized Databases." Journal of Proteome Research 12, no. 7 (June 6, 2013): 3215–22. http://dx.doi.org/10.1021/pr4000625.

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Ndiaye, Massamba M., Ha Phuong Ta, Giovanni Chiappetta, and Joëlle Vinh. "Correction to “On-Chip Sample Preparation Using a ChipFilter Coupled to NanoLC-MS/MS for Bottom-Up Proteomics”." Journal of Proteome Research 20, no. 12 (November 3, 2021): 5424. http://dx.doi.org/10.1021/acs.jproteome.1c00846.

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